ID A0A1Y3YD77_9FIRM Unreviewed; 1186 AA.
AC A0A1Y3YD77;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN ORFNames=B5G00_05485 {ECO:0000313|EMBL:OUN93387.1};
OS Blautia sp. An46.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Blautia.
OX NCBI_TaxID=1965636 {ECO:0000313|EMBL:OUN93387.1, ECO:0000313|Proteomes:UP000196301};
RN [1] {ECO:0000313|Proteomes:UP000196301}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An46 {ECO:0000313|Proteomes:UP000196301};
RA Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA Rychlik I.;
RT "Function of individual gut microbiota members based on whole genome
RT sequencing of pure cultures obtained from chicken caecum.";
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Required for chromosome condensation and partitioning.
CC {ECO:0000256|HAMAP-Rule:MF_01894}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01894}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01894}.
CC -!- DOMAIN: Contains large globular domains required for ATP hydrolysis at
CC each terminus and a third globular domain forming a flexible hinge near
CC the middle of the molecule. These domains are separated by coiled-coil
CC structures. {ECO:0000256|HAMAP-Rule:MF_01894}.
CC -!- SIMILARITY: Belongs to the SMC family. SMC3 subfamily.
CC {ECO:0000256|ARBA:ARBA00005917}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OUN93387.1}.
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DR EMBL; NFIF01000005; OUN93387.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y3YD77; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000196301; Unassembled WGS sequence.
DR GO; GO:0005694; C:chromosome; IEA:InterPro.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030261; P:chromosome condensation; IEA:InterPro.
DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-UniRule.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
DR GO; GO:0007062; P:sister chromatid cohesion; IEA:InterPro.
DR CDD; cd03278; ABC_SMC_barmotin; 2.
DR Gene3D; 1.10.287.1490; -; 1.
DR Gene3D; 1.20.1060.20; -; 1.
DR Gene3D; 3.30.70.1620; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR HAMAP; MF_01894; Smc_prok; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR003395; RecF/RecN/SMC_N.
DR InterPro; IPR024704; SMC.
DR InterPro; IPR010935; SMC_hinge.
DR InterPro; IPR036277; SMC_hinge_sf.
DR InterPro; IPR011890; SMC_prok.
DR NCBIfam; TIGR02168; SMC_prok_B; 1.
DR PANTHER; PTHR43977; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN 3; 1.
DR PANTHER; PTHR43977:SF1; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN 3; 1.
DR Pfam; PF06470; SMC_hinge; 1.
DR Pfam; PF02463; SMC_N; 1.
DR PIRSF; PIRSF005719; SMC; 1.
DR SMART; SM00968; SMC_hinge; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF75553; Smc hinge domain; 1.
DR SUPFAM; SSF57997; Tropomyosin; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01894};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|HAMAP-
KW Rule:MF_01894};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01894};
KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_01894};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01894};
KW Reference proteome {ECO:0000313|Proteomes:UP000196301}.
FT DOMAIN 521..638
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT COILED 167..201
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 227..471
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 672..888
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 917..994
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT BINDING 32..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
SQ SEQUENCE 1186 AA; 137334 MW; 1C4CC0388D74A892 CRC64;
MYLKSIDVQG FKSFANKITF EFHNGITAIV GPNGSGKSNV ADAVRWVLGE QSAKQLRGGN
MQDVIFSGTE TRKPLGFAYV AITLDNSDHK LPIDYQEVTI ARRLYRSGES EYLLNGTACR
LKDVNELFYD TGIGKEGYSI IGQGQIDKIL SGKPEERREL FDEAAGIVKF KRRKNTALKK
LEEEQQNLTR VRDILGELSR QLVPLEKQSE TARVYLKKKE TLKQLDIQMF LAEMERIRSQ
MKETEGKYQI VQSDLEETAK DFETTRTEYD RLEKELEKLE EEIQAAREES TEKTLKKQQL
ENQIHILQEQ INSGRQRDIQ YEDRMKNLEE DLEKRREEAE KCQAEKAELA EKIKAFQKSL
EETQGTFKDT AMEIHSLEEK VERDKNEIIE ILNLRASTKG KLQRYDTMME QNSLRRTELN
QKYLTLKSEA AKLQDSGEKY LEEKKEIEET IEKLIRQGNR CEDQIKKYQA EISRGNQQLE
VGQTAYHREA SRLESLRNIT ERYDGYGNSI RRVMEQKKRV PGIRGVVADI LKVEKEYETA
IETALGGSIQ NIVTDNEETA KELISFLKKN KYGRATFLPL TSMNNKKPLN NPQALGEPGV
IGIASDLVKV AQEYQGLAVY LLGRTLVVDH IDHGIAIARK YHYSIRMVTL EGESLNPGGS
LTGGSFKNNS NLLGRRREIE ELQDAVEKLK KDMEDMQKKL EEYRNKRNQC RDQSASIQEQ
LQEQYIRENT VQVNLDSMGG KKEEIRKEYE SLKLEKEDLE KQIREIRENT SSIQLELETS
DSQEKYLEEE INKNQTLLEE KKKKEAEISA SLEKIHLESA GFTSRQGFVL ENLNRIREEI
MNFERQKDSL RASMEQGKED ILQKEKEISQ LKETIKAGEE ETRRDQEKMK EALGRKEEMT
REHKGFFARR DELSSRMNLL DKESYRLQGQ KEKLEEEQES QTNYMWEEYE LTYGQAKEQA
LEETKERNEI KKEIQQIKTE IRQLGNVNVN AIEEYKEISQ RHDFMKTQHE DLVKSEETLL
GIIQELDTGM RRQFEEKFAQ IRTEFDKAFK ELFGGGKGTI ELDEEEDILE AGIRIISQPP
GKKLQNMMQL SGGEKALTAI ALLFAIQNLK PSPFCLLDEI EAALDDSNVT RYAQYLHKLT
KNTQFIIITH RRGTMTAADR LYGITMQEKG VSTLVSVDLI ERDLDK
//
